2IHR

RF2 of Thermus thermophilus

2IHR の概要

• エントリーDOI: 10.2210/pdb2ihr/pdb
• 分子名称: Peptide chain release factor 2 (2 entities in total)
• 機能のキーワード: mixed alpha-beta, translation
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41359.82

構造登録者

Dobbek, H.,Voertler, C.S.,Sprinzl, M. (登録日: 2006-09-27, 公開日: 2007-02-20, 最終更新日: 2023-08-30)

主引用文献

Zoldak, G.,Redecke, L.,Svergun, D.I.,Konarev, P.V.,Voertler, C.S.,Dobbek, H.,Sedlak, E.,Sprinzl, M.
Release factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies.
Nucleic Acids Res., 35:1343-1353, 2007

PubMed Abstract: Prokaryotic class I release factors (RFs) respond to mRNA stop codons and terminate protein synthesis. They interact with the ribosomal decoding site and the peptidyl-transferase centre bridging these 75 A distant ribosomal centres. For this an elongated RF conformation, with partially unfolded core domains II.III.IV is required, which contrasts the known compact RF crystal structures. The crystal structure of Thermus thermophilus RF2 was determined and compared with solution structure of T. thermophilus and Escherichia coli RF2 by microcalorimetry, circular dichroism spectroscopy and small angle X-ray scattering. The structure of T. thermophilus RF2 in solution at 20 degrees C is predominantly compact like the crystal structure. Thermodynamic analysis point to an initial melting of domain I, which is independent from the melting of the core. The core domains II.III.IV melt cooperatively at the respective physiological temperatures for T. thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome.

PubMed: 17272297
DOI: 10.1093/nar/gkl696

実験手法

X-RAY DIFFRACTION (2.5 Å)